Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structural dynamics of the DnaK-peptide complex.

Simone Popp1, Lars Packschies, Nicole Radzwill

  • 1Department of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany.

Journal of Molecular Biology
|March 24, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Assessing the problem of excitation light scattering in high-viscosity jets used in serial crystallography sample delivery.

Journal of applied crystallography·2026
Same author

SNAP-tag2 for faster and brighter protein labeling.

Nature chemical biology·2025
Same author

Discovery of selective low molecular weight interleukin-36 receptor antagonists by encoded library technologies.

Nature communications·2025
Same author

Two-Photon-Driven Photoprotection Mechanism in Echinenone-Functionalized Orange Carotenoid Protein.

Journal of the American Chemical Society·2025
Same author

Discovery and development of ANV419, an IL-2/anti-IL-2 antibody fusion protein with potent CD8+ T and natural killer cell-stimulating capacity for cancer immunotherapy.

mAbs·2024
Same author

Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review.

Nanomaterials (Basel, Switzerland)·2022
Same journal

BindRNAgen: Protein-binding RNA sequence generation using latent diffusion models.

Journal of molecular biology·2026
Same journal

Structural basis of HSP90C, a highly active chloroplastic HSP90 chaperone from Arabidopsis thaliana.

Journal of molecular biology·2026
Same journal

Clinical inflammasome biomarkers: Progress and prospects.

Journal of molecular biology·2026
Same journal

Biologically Relevant, Cationic Residues in Human Rhinovirus Stabilize Capsid-Bound RNA Duplexes, and Restrict Capsid Flexibility.

Journal of molecular biology·2026
Same journal

Cryo-EM structures of phage T4 infection intermediate.

Journal of molecular biology·2026
Same journal

A classic fold with a twist: Structural architecture of Dhillonvirus phage Bas18.

Journal of molecular biology·2026
See all related articles

The molecular chaperone DnaK

Area of Science:

  • Molecular biology
  • Protein dynamics
  • Biochemistry

Background:

  • The molecular chaperone DnaK binds unfolded proteins via a seven-amino-acid stretch.
  • DnaK's nucleotide state (ATP or ADP) regulates substrate binding kinetics.
  • The C-terminal LID domain's mobility influences peptide binding dynamics.

Purpose of the Study:

  • To investigate nucleotide-dependent structural changes in DnaK's peptide-binding region.
  • To determine if ATP hydrolysis induces structural changes in bound peptides.
  • To link structural changes to peptide binding kinetics.

Main Methods:

  • Synthesized model peptides with two cysteine residues.
  • Labeled peptides with electron spin probes.
  • Utilized electron paramagnetic resonance (EPR) spectroscopy to measure distances and mobilities.

Related Experiment Videos

Main Results:

  • No significant changes in spin label mobility or distance were observed in bound peptides.
  • EPR measurements indicated no nucleotide-dependent structural alterations in the central peptide region.
  • The results suggest DnaK's ATPase activity does not directly alter the peptide-binding pocket structure.

Conclusions:

  • Nucleotide-dependent structural changes in DnaK do not occur within the peptide-binding pocket.
  • The ATPase activity primarily affects the LID domain or more distant residues.
  • Structural plasticity of the peptide-binding region is not directly modulated by nucleotide state.